An approach to optimizing the active site in a glutathione transferase by evolution in vitro.

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Article

An approach to optimizing the active site in a glutathione transferase by evolution in vitro.

The Biochemical journal - 15 Nov 1999

Hansson L O, Widersten M, Mannervik B

Abstract excerpt

A glutathione transferase (GST) mutant with four active-site substitutions (Phe(10)-->Pro/Ala(12)-->Trp/Leu(107)-->Phe/Leu(108)-->Arg) (C36) was isolated from a library of active-site mutants of human GST A1-1 by the combination of phage display and mechanism-based affinity adsorption [Hansson, W...

Topics

Amino Acid Substitution
Base Sequence
Catalytic Domain
DNA Primers
Dinitrochlorobenzene
Directed Molecular Evolution
Genetic Variation
Glutathione Transferase
Humans
In Vitro Techniques
Kinetics
Models, Molecular
Mutagenesis, Site-Directed
Protein Structure, Secondary
Substrate Specificity

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Identifiers

PMID: 10548538
PMCID: PMC1220618

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-10548538-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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